Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance.
J Mol Biol
; 430(17): 2677-2687, 2018 08 17.
Article
in En
| MEDLINE
| ID: mdl-29886014
ABSTRACT
One of the most critical steps of protein biosynthesis is the coupled movement of mRNA, which encodes genetic information, with tRNAs on the ribosome. In eukaryotes, this process is catalyzed by a conserved G-protein, the elongation factor 2 (eEF2), which carries a unique post-translational modification, called diphthamide, found in all eukaryotic species. Here we present near-atomic resolution cryo-electron microscopy structures of yeast 80S ribosome complexes containing mRNA, tRNA and eEF2 trapped in different GTP-hydrolysis states which provide further structural insights into the role of diphthamide in the mechanism of translation fidelity in eukaryotes.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Ribosomes
/
Saccharomyces cerevisiae
/
Protein Biosynthesis
/
RNA, Messenger
/
RNA, Transfer
/
Peptide Elongation Factor 2
/
Guanosine Triphosphate
/
Histidine
Type of study:
Prognostic_studies
Language:
En
Journal:
J Mol Biol
Year:
2018
Document type:
Article
Affiliation country: